ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Polyamine-modulated factor 1

Intermolecular
Cysteine 63 of Protein MIS12 homolog and cysteine 61 L
Cysteine 63 of Protein MIS12 homolog and cysteine 64 L
Intramolecular
Cysteine 61 and cysteine 64 L
A redox-regulated disulphide may form between cysteine 63 of Protein MIS12 homolog and cysteine 61 of Polyamine-modulated factor 1.

Details

Redox score ?
72
PDB code
5lsj
Structure name
crystal structure of the human kinetochore mis12-cenp-c delta-head2 complex
Structure deposition date
2016-09-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
51
Peptide A name
Protein MIS12 homolog
Peptide B name
Polyamine-modulated factor 1
Peptide A accession
Q9H081
Peptide B accession
Q6P1K2
Peptide A residue number
63
Peptide B residue number
61

Ligandability

Cysteine 63 of Protein MIS12 homolog

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 61 of Polyamine-modulated factor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 63 of Protein MIS12 homolog and cysteine 64 of Polyamine-modulated factor 1.

Details

Redox score ?
62
PDB code
5lsk
Structure name
crystal structure of the human kinetochore mis12-cenp-c complex
Structure deposition date
2016-09-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
47
Peptide A name
Protein MIS12 homolog
Peptide B name
Polyamine-modulated factor 1
Peptide A accession
Q9H081
Peptide B accession
Q6P1K2
Peptide A residue number
63
Peptide B residue number
64

Ligandability

Cysteine 63 of Protein MIS12 homolog

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 64 of Polyamine-modulated factor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Polyamine-modulated factor 1 between cysteines 61 and 64. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
5lsj
Structure name
crystal structure of the human kinetochore mis12-cenp-c delta-head2 complex
Structure deposition date
2016-09-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
38
Peptide accession
Q6P1K2
Residue number A
61
Residue number B
64
Peptide name
Polyamine-modulated factor 1

Ligandability

Cysteine 61 of Polyamine-modulated factor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 64 of Polyamine-modulated factor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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